VTC3_YEAST
ID VTC3_YEAST Reviewed; 835 AA.
AC Q02725; D6W3Z3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Vacuolar transporter chaperone 3;
DE AltName: Full=Phosphate metabolism protein 2;
GN Name=VTC3; Synonyms=PHM2; OrderedLocusNames=YPL019C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 7-16; 28-62; 101-112; 149-175; 194-221; 227-252;
RP 265-284; 330-340; 342-358; 363-386; 398-419; 425-447; 466-477; 481-495 AND
RP 808-835, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
RP INDUCTION.
RX PubMed=11102525; DOI=10.1091/mbc.11.12.4309;
RA Ogawa N., DeRisi J.L., Brown P.O.;
RT "New components of a system for phosphate accumulation and polyphosphate
RT metabolism in Saccharomyces cerevisiae revealed by genomic expression
RT analysis.";
RL Mol. Biol. Cell 11:4309-4321(2000).
RN [5]
RP FUNCTION, IDENTIFICATION IN VTC COMPLEX, SUBUNIT, AND INTERACTION WITH NYV1
RP AND VPH1.
RX PubMed=11823419; DOI=10.1093/emboj/21.3.259;
RA Mueller O., Bayer M.J., Peters C., Andersen J.S., Mann M., Mayer A.;
RT "The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-
RT complex formation.";
RL EMBO J. 21:259-269(2002).
RN [6]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=12584253; DOI=10.1242/jcs.00328;
RA Mueller O., Neumann H., Bayer M.J., Mayer A.;
RT "Role of the Vtc proteins in V-ATPase stability and membrane trafficking.";
RL J. Cell Sci. 116:1107-1115(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-198; SER-270;
RP SER-592; SER-621 AND SER-622, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND SER-592, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183; SER-198; SER-274;
RP SER-621 AND SER-622, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45; SER-50; SER-195;
RP SER-198; SER-270; SER-274; SER-621 AND SER-622, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP FUNCTION, AND DOMAIN.
RX PubMed=27080106; DOI=10.1126/science.aad9858;
RA Wild R., Gerasimaite R., Jung J.Y., Truffault V., Pavlovic I., Schmidt A.,
RA Saiardi A., Jessen H.J., Poirier Y., Hothorn M., Mayer A.;
RT "Control of eukaryotic phosphate homeostasis by inositol polyphosphate
RT sensor domains.";
RL Science 352:986-990(2016).
CC -!- FUNCTION: Component of the vacuolar transporter chaperone (VTC)
CC complex, which plays a role in vacuolar membrane fusion. Required for
CC LMA1 release prior to membrane fusion (PubMed:11823419). Binds inositol
CC hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as
CC 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important
CC intracellular signaling molecules (PubMed:27080106). Inositol
CC polyphosphate binding promotes vacuolar polyphosphate synthesis
CC (PubMed:27080106). {ECO:0000269|PubMed:11823419,
CC ECO:0000269|PubMed:27080106}.
CC -!- SUBUNIT: The VTC complex is an integral membrane heterooligomer
CC composed of VTC1, VTC2, VTC3 and VTC4. The complex interacts with the
CC v-SNARE NYV1 and with the V(0) subunit of V-ATPase VPH1.
CC {ECO:0000269|PubMed:11823419}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12584253};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12584253}.
CC -!- INDUCTION: By low phosphate. {ECO:0000269|PubMed:11102525}.
CC -!- DOMAIN: The SPX domain has very high affinity for inositol
CC polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-
CC myo-inositol pentakisphosphate (5-InsP7), and moderate affinity for
CC inorganic pyrophosphate. Its affinity for inorganic phosphate is tow to
CC three orders of magnitude lower. {ECO:0000305|PubMed:27080106}.
CC -!- MISCELLANEOUS: Present with 2630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VTC2/3 family. {ECO:0000305}.
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DR EMBL; U36624; AAB68168.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11409.1; -; Genomic_DNA.
DR PIR; S63463; S63463.
DR RefSeq; NP_015306.1; NM_001183833.1.
DR AlphaFoldDB; Q02725; -.
DR SMR; Q02725; -.
DR BioGRID; 36158; 78.
DR ComplexPortal; CPX-784; Vacuolar transporter chaperone complex.
DR DIP; DIP-2000N; -.
DR IntAct; Q02725; 6.
DR MINT; Q02725; -.
DR STRING; 4932.YPL019C; -.
DR TCDB; 4.E.1.1.2; the vacuolar (acidocalcisome) polyphosphate polymerase (v-ppp) family.
DR CarbonylDB; Q02725; -.
DR iPTMnet; Q02725; -.
DR MaxQB; Q02725; -.
DR PaxDb; Q02725; -.
DR PRIDE; Q02725; -.
DR EnsemblFungi; YPL019C_mRNA; YPL019C; YPL019C.
DR GeneID; 856088; -.
DR KEGG; sce:YPL019C; -.
DR SGD; S000005940; VTC3.
DR VEuPathDB; FungiDB:YPL019C; -.
DR eggNOG; KOG1161; Eukaryota.
DR eggNOG; KOG4580; Eukaryota.
DR GeneTree; ENSGT00940000176481; -.
DR HOGENOM; CLU_009308_2_0_1; -.
DR InParanoid; Q02725; -.
DR OMA; YSYERRI; -.
DR BioCyc; YEAST:YPL019C-MON; -.
DR PRO; PR:Q02725; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02725; protein.
DR GO; GO:0000421; C:autophagosome membrane; IC:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0033254; C:vacuolar transporter chaperone complex; IPI:SGD.
DR GO; GO:0005516; F:calmodulin binding; IDA:SGD.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:UniProtKB.
DR GO; GO:0061736; P:engulfment of target by autophagosome; IC:ComplexPortal.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; IMP:UniProtKB.
DR GO; GO:0016237; P:lysosomal microautophagy; IDA:SGD.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006797; P:polyphosphate metabolic process; IMP:SGD.
DR GO; GO:0007034; P:vacuolar transport; IDA:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR Gene3D; 3.20.100.30; -; 1.
DR InterPro; IPR003807; DUF202.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR018966; VTC_domain.
DR InterPro; IPR042267; VTC_sf.
DR Pfam; PF02656; DUF202; 1.
DR Pfam; PF09359; VTC; 1.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..835
FT /note="Vacuolar transporter chaperone 3"
FT /id="PRO_0000065936"
FT TOPO_DOM 1..709
FT /note="Cytoplasmic"
FT TRANSMEM 710..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..735
FT /note="Vacuolar"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..778
FT /note="Cytoplasmic"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..835
FT /note="Vacuolar"
FT DOMAIN 1..145
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT REGION 126..133
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000305|PubMed:27080106"
FT REGION 564..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 385..413
FT /evidence="ECO:0000255"
FT COMPBIAS 616..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 22
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT SITE 26
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 835 AA; 96553 MW; F098B36A9D9B9C11 CRC64;
MLFGIKLAND VYPPWKDSYI DYERLKKLLK ESVIHDGRSS VDSWSERNES DFVEALDKEL
EKVYTFQISK YNAVLRKLDD LEENTKSAEK IQKINSEQFK NTLEECLDEA QRLDNFDRLN
FTGFIKIVKK HDKLHPNYPS VKSLLQVRLK ELPFNNSEEY SPLLYRISYL YEFLRSNYDH
PNTVSKSLAS TSKLSHFSNL EDASFKSYKF WVHDDNIMEV KARILRHLPA LVYASVPNEN
DDFVDNLESD VRVQPEARLN IGSKSNSLSS DGNSNQDVEI GKSKSVIFPQ SYDPTITTLY
FDNDFFDLYN NRLLKISGAP TLRLRWIGKL LDKPDIFLEK RTFTENTETG NSSFEEIRLQ
MKAKFINNFI FKNDPSYKNY LINQLRERGT QKEELEKLSR DFDNIQNFIV EEKLQPVLRA
TYNRTAFQIP GDQSIRVTID SNIMYIREDS LDKNRPIRNP ENWHRDDIDS NIPNPLRFLR
AGEYSKFPYS VMEIKVINQD NSQMPNYEWI KDLTNSHLVN EVPKFSLYLQ GVASLFGEDD
KYVNILPFWL PDLETDIRKN PQEAYEEEKK TLQKQKSIHD KLDNMRRLSK ISVPDGKTTE
RQGQKDQNTR HVIADLEDHE SSDEEGTALP KKSAVKKGKK FKTNAAFLKI LAGKNISENG
NDPYSDDTDS ASSFQLPPGV KKPVHLLKNA GPVKVEAKVW LANERTFNRW LSVTTLLSVL
TFSIYNSVQK AEFPQLADLL AYVYFFLTLF CGVWAYRTYL KRLTLIKGRS GKHLDAPVGP
ILVAVVLIVT LVVNFSVAFK EAARRERGLV NVSSQPSLPR TLKPIQDFIF NLVGE
